BackgroundHistone H4- along with H2A, H2B, and H3- is involved in the structure of chromatin in eukaryotic cells. Histone H4 can undergo several different types of epigenetic modifications that influence cellular processes. These modifications including acetylation, phosphorylation, methylation, ubiquitination, and ADP-ribosylation, occur on the N-terminal tail domains of histone H4, which results in remodeling of the nucleosome structure into an open conformation more accessible to transcription complexes. In most species, histone H4 is primarily acetylated at lysine 5, 8, 12, and 16.

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